The Liprin homology domain is essential for the homomeric interaction of SYD-2/Liprin-α protein in presynaptic assembly
Open accessAbstract
Synapses are asymmetric structures that are specialized for neuronal signal transduction. A unique set of proteins is present at the presynaptic active zone, which is a core structure essential for neurotransmitter release. In Caenorhabditis elegans HSN neurons, SYD-2, a Liprin-α family protein, acts together with a GAP protein SYD-1 to promote presynaptic assembly. Previous studies have shown that elevating the activity of syd-2 can bypass the requirement of syd-1. Liprin-α proteins are composed of coiled-coil-rich regions in the N-terminal half, which mediate interactions with adapter proteins at the presynaptic active zone, and three SAM domains in the C terminus, which bind proteins such as LAR receptor tyrosine phosphatase. To address the molecular mechanism by which SYD-2 activity is regulated, we performed structure–function studies. By monitoring the ability of SYD-2 transgenes to rescue syd-2(lf)and to suppress syd-1(lf)phenotypes in HSN neuron synapses, we identified the N-terminal half of SYD-2 as minimally required for rescuing syd-2(lf)phenotypes. A highly conserved short coiled-coil segment named Liprin Homology 1 (LH1) domain is both necessary and sufficient to suppress syd-1(lf)defects. We show that the LH1 domain forms a dimer and promotes further oligomerization and/or complex formation of SYD-2/Liprin-α proteins. The role of the LH1 domain in presynaptic assembly can be partially complemented by artificial dimerization. These findings suggest a model by which the self-assembly of SYD-2/Liprin-α proteins mediated by the coiled-coil LH1 domain is one of the key steps to the accumulation of presynaptic components at nascent synaptic junctions.
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α-Liprin is required for active zone formation with recruitment of synaptic vesicles and of LAR-type receptor phosphotyrosine phosphatases.
“Together, these data established that active zone formation with recruitment of synaptic vesicles and of LAR-type receptor phosphotyrosine phosphatases requires α-liprin, possibly by simultaneous binding of α-liprin to the receptor phosphotyrosine phosphatase, RIM, ELKS, Syd-1, and itself.”
From The Presynaptic Active Zone (2012) · cites this paper as Taru and Jin, 2011
The Results section (‘LH1 domain is necessary for SYD-2 function in presynaptic assembly’; page unavailable) reports that loss of SYD-2 greatly diminishes synaptic-vesicle and active-zone markers in C. elegans HSN neurons. The Introduction says Liprin-α binds LAR-type receptor phosphatases, but the paper does not establish that Liprin-α is required to recruit those phosphatases to active zones. (LLM, conf=0.87)
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- Authors
- Taru, H., & Jin, Y.
- Affiliations
- Hokkaido University (JP)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Taru, Hidenori
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2011-11-09
- Volume
- 31
- Issue
- 45
- Pages
- 16261-16268
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC3500560
- OpenAlex
- W2159271716
- Cited by
- 49
- References
- 28
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2023: 5 · 2022: 2 · 2021: 5 · 2020: 2 · 2019: 5 · 2018: 2 · 2017: 2 · 2016: 2 · 2015: 4 · 2014: 4 · 2013: 7 · 2012: 3
- FWCI
- 1.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Hokkaido University Collection of Scholarly and Academic Papers (Hokkaido University) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Suzuken Memorial Foundation
- Akiyama Life Science Foundation
- Hokkaido University
- National Institutes of Health (NS035546)
- University of California, San Diego
- Japan Society for the Promotion of Science (23790070)
- National Institute of Neurological Disorders and Stroke (R37NS035546, NS 035546, R01NS035546)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neurobiology and Insect Physiology Research
- Keywords
- Liprin-α, coiled-coil domain, Caenorhabditis elegans, protein dimerization, structure-function analysis
- MeSH terms
- Animals, Cell Line, Transformed, Chlorocebus aethiops, Gene Expression Regulation, Humans, Motor Neurons, Mutation, Phosphoproteins, Synapses, Caenorhabditis elegans, Protein Structure, Tertiary, Presynaptic Terminals, Caenorhabditis elegans Proteins, Animals, Genetically Modified, Intercellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Green Fluorescent Proteins
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